DCK_BOVIN
ID DCK_BOVIN Reviewed; 260 AA.
AC Q3MHR2;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Deoxycytidine kinase;
DE Short=dCK;
DE EC=2.7.1.74 {ECO:0000250|UniProtKB:P27707};
DE AltName: Full=Deoxyadenosine kinase;
DE EC=2.7.1.76 {ECO:0000250|UniProtKB:P27707};
DE AltName: Full=Deoxyguanosine kinase;
DE EC=2.7.1.113 {ECO:0000250|UniProtKB:P27707};
GN Name=DCK;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Phosphorylates the deoxyribonucleosides deoxycytidine,
CC deoxyguanosine and deoxyadenosine. {ECO:0000250|UniProtKB:P27707}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a
CC ribonucleoside 5'-diphosphate + dCMP + H(+); Xref=Rhea:RHEA:20061,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15698, ChEBI:CHEBI:57566,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=2.7.1.74;
CC Evidence={ECO:0000250|UniProtKB:P27707};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + ATP = ADP + dAMP + H(+);
CC Xref=Rhea:RHEA:23452, ChEBI:CHEBI:15378, ChEBI:CHEBI:17256,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58245, ChEBI:CHEBI:456216;
CC EC=2.7.1.76; Evidence={ECO:0000250|UniProtKB:P27707};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + ATP = ADP + dGMP + H(+);
CC Xref=Rhea:RHEA:19201, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57673, ChEBI:CHEBI:456216;
CC EC=2.7.1.113; Evidence={ECO:0000250|UniProtKB:P27707};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P27707}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P27707}.
CC -!- PTM: Phosphorylated and activated in vitro upon phosphorylation at Ser-
CC 74 by CSNK1D/CK1. {ECO:0000250|UniProtKB:P27707}.
CC -!- SIMILARITY: Belongs to the DCK/DGK family. {ECO:0000305}.
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DR EMBL; BC105141; AAI05142.1; -; mRNA.
DR RefSeq; NP_001029745.1; NM_001034573.1.
DR AlphaFoldDB; Q3MHR2; -.
DR SMR; Q3MHR2; -.
DR STRING; 9913.ENSBTAP00000016449; -.
DR PaxDb; Q3MHR2; -.
DR PRIDE; Q3MHR2; -.
DR Ensembl; ENSBTAT00000016449; ENSBTAP00000016449; ENSBTAG00000012397.
DR GeneID; 530642; -.
DR KEGG; bta:530642; -.
DR CTD; 1633; -.
DR VEuPathDB; HostDB:ENSBTAG00000012397; -.
DR VGNC; VGNC:27914; DCK.
DR eggNOG; KOG4235; Eukaryota.
DR GeneTree; ENSGT00940000157321; -.
DR HOGENOM; CLU_030466_1_1_1; -.
DR InParanoid; Q3MHR2; -.
DR OMA; YQDWHEW; -.
DR OrthoDB; 1505356at2759; -.
DR TreeFam; TF324413; -.
DR Reactome; R-BTA-73614; Pyrimidine salvage.
DR Reactome; R-BTA-74217; Purine salvage.
DR Proteomes; UP000009136; Chromosome 6.
DR Bgee; ENSBTAG00000012397; Expressed in thymus and 105 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043771; F:cytidine kinase activity; IEA:Ensembl.
DR GO; GO:0004136; F:deoxyadenosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004137; F:deoxycytidine kinase activity; IBA:GO_Central.
DR GO; GO:0004138; F:deoxyguanosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0019136; F:deoxynucleoside kinase activity; IBA:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0106383; P:dAMP salvage; IEA:Ensembl.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; ISS:UniProtKB.
DR CDD; cd01673; dNK; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR002624; DCK/DGK.
DR InterPro; IPR031314; DNK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF01712; dNK; 1.
DR PIRSF; PIRSF000705; DNK; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transferase.
FT CHAIN 1..260
FT /note="Deoxycytidine kinase"
FT /id="PRO_0000295028"
FT ACT_SITE 127
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT BINDING 28..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 188..192
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 240..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 11
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27707"
FT MOD_RES 15
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27707"
FT MOD_RES 72
FT /note="Phosphothreonine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27707"
FT MOD_RES 74
FT /note="Phosphoserine; by CK1"
FT /evidence="ECO:0000250|UniProtKB:P27707"
SQ SEQUENCE 260 AA; 30329 MW; 07EB33EA77A8F457 CRC64;
MATPPKRSCP SPAASSEGTR IKKISIEGNI AAGKSTFVNI LKQVCEDWEV VPEPVARWCN
VQSTQDEFEE LTTSQKSGGN VLQMMYEKPE RWSFTFQSYA CLSRIRAQLA ALNGKLKDAE
KPVLFFERSV YSDRYIFASN LYESDCMNET EWTIYQDWHD WMNNQFGQSL ELDGIIYLRA
TPEKCLNRIY LRGRNEEQGI PLEYLEKLHY KHESWLLHRT LKTNFDYLQE VPILTLDVNE
DFKDKHDSLI EKVKDFLSTL
